Clusterin Prevents Aggregation of Neuropeptide 106-126 in Vitro

Clusterin Prevents Aggregation of Neuropeptide 106-126 in Vitro

The prion/amyloid neuropeptide 106-126 spontaneously aggregates to form fibrillar structures in vitro. The aggregation in vitro could be prevented in a dose-related manner by clusterin, and the specificity of this action was confirmed by reversal with antibody to clusterin. The relevance of these ob...

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Veröffentlicht in:Biochemical and biophysical research communications 1999-06, Vol.259 (2), p.336-340
Hauptverfasser: McHattie, S., Edington, N.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Animals
Antibodies - immunology
Clusterin
Encephalopathy, Bovine Spongiform - metabolism
Glycoproteins - immunology
Glycoproteins - pharmacology
In Vitro Techniques
Microscopy, Electron
Molecular Chaperones
Molecular Sequence Data
Neuropeptides - chemical synthesis
Neuropeptides - chemistry
Peptide Fragments - chemical synthesis
Peptide Fragments - chemistry
Prions - chemical synthesis
Prions - chemistry
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Zusammenfassung:The prion/amyloid neuropeptide 106-126 spontaneously aggregates to form fibrillar structures in vitro. The aggregation in vitro could be prevented in a dose-related manner by clusterin, and the specificity of this action was confirmed by reversal with antibody to clusterin. The relevance of these observations is discussed in relation to previous observations that clusterin and PrPBSE colocalise in naturally occurring cases of BSE.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1999.0781